Effects of diacylglycerols on the structure of phosphatidylcholine bilayers: a deuterium and phosphorus-31 NMR study

Boeck, Hilde De; Zidovetzki, Raphael

doi:10.1021/bi00444a043

Cited by 80 publications

(60 citation statements)

References 51 publications

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“…A variety of evidence supports the conclusion that certain diglycerides enhance PLAz-catalyzed hydrolysis of phospholipid bilayers because of the tendency of the glyceride to form domains within the bilayer (Cunningham et al, 1989;Zidovetzki et al, 1992;De Boeck & Zidovetzki, 1992). The observations reported in this paper support that interpretation and extend it with data on C-16 MAG and C-16 TAG.…”

Section: Discussionsupporting

confidence: 86%

Effects of Temperature and Glycerides on the Enhancement of Agkistrodon piscivorus piscivorus Phospholipase A2 Activity by Lysolecithin and Palmitic Acid

Bell

Baker²,

Bent³

et al. 1995

Biochemistry

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The effect of temperature and various glycerides to modulate the ability of lysolecithin and fatty acid to promote high phospholipase A2 activity was studied using dipalmitoylphosphatidylcholine large unilamellar vesicles as substrate. The length of the lag phase prior to the accumulation of sufficient hydrolysis products (lysolecithin and fatty acid) to support high phospholipase activity was shortest at temperatures near the thermotropic phase transition of the phospholipid substrate. A reduction in the lag phase correlated with a reduction in the requirement for hydrolysis products at the phase transition temperature, where the bilayer exists in a state of fluctuating domains of gel and liquid crystal. Dipalmitoylglycerol and tripalmitoylglycerol also reduced the length of the lag phase. This reduction was both concentration-dependent and temperature-dependent relative to the phase transition in the presence of the glycerides. As with the effect of temperature, the ability of di- and triglycerides to decrease the lag time correlated with a decrease in the amount of reaction products necessary to promote high phospholipase activity. This effect coincided with the tendency of the glycerides to form domains in the bilayer. Glycerides that did not form domains either had no effect (monopalmitoylglycerol) or increased the length of the lag phase (dicaprylglycerol). These data suggest that the effect of the reaction products to increase phospholipase A2 activity is aided by the presence of fluctuations in lipid domains within the bilayer.

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Section: Discussionsupporting

confidence: 86%

Effects of Temperature and Glycerides on the Enhancement of Agkistrodon piscivorus piscivorus Phospholipase A2 Activity by Lysolecithin and Palmitic Acid

Bell

Baker²,

Bent³

et al. 1995

Biochemistry

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“…It could be taken up intact or it could be first broken down by a lipase and then FFA could be taken up (see above). DAG was found to be dangerous to the structure of membranes (Das and Rand, 1986;De Boeck and Zidovetzki, 1989), however, with a DAG transporter this might not be a problem. In M. sexta the transport of DAG out of cells (not in), is assumed for fat body (Van Heusden and Law, 1989) and gut (Canavoso and Wells, 2000;Arrese et al, 2001).…”

Section: Uptake Of Dagmentioning

confidence: 88%

Lipid uptake by insect oocytes

Ziegler

Antwerpen

2006

Insect Biochemistry and Molecular Biology

202

172

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“…A lag time is observed in phospholipase A 2 under a variety of conditions, until a certain fraction of the reaction products, free fatty acids and lysolecithin, accumulates in the bilayer (33)(34)(35)43), just like PLC. Phospholipase A 2 activation by long-chain DAG has already been mentioned above (31,32) as well as the role of bilayer microheterogeneities in promoting the burst of activity of this enzyme (14).…”

Section: Phospholipase C and Mixed Bilayersmentioning

confidence: 95%

Phospholipase C Hydrolysis of Phospholipids in Bilayers of Mixed Lipid Compositions

Alonso

1998

Biochemistry

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Phosphatidylcholine phospholipase C (EC 3.1.4.3) from Bacillus cereus has been assayed with substrates in the form of large unilamellar vesicles. Phosphatidylcholine, phosphatidylethanolamine (also a substrate for the enzyme), sphingomyelin, and cholesterol have been mixed in various proportions, in binary, ternary, and quaternary mixtures. A lag period, followed by a burst of enzyme activity, has been found in all cases. The activity burst was always accompanied by an increase in turbidity of the vesicle suspension. Varying lipid compositions while keeping constant all the other parameters leads to a range of lag times extending over 2 orders of magnitude (from 0.13 to 38.0 min), and a similar variability is found in maximal enzyme rates (from 0.40 to 55.9 min-1). Meanwhile, the proportion of substrate that is hydrolyzed during the lag period remains relatively constant at 0.10% moles of total lipid, in agreement with the idea that enzyme activation is linked to vesicle aggregation through diacylglycerol-rich patches. Phosphatidylethanolamine and cholesterol enhance the enzyme activity in a dose-dependent way: they reduce the lag times and increase the maximal rates. The opposite is true of sphingomyelin. These lipids exert each its own peculiar effect, positive or negative, either alone or in combination, so that the susceptibility of a given mixture to the enzyme activity can be to some extent predicted from its composition. Phospholipase C activity is not directly influenced by the formation of nonlamellar structures. However, the presence of lipids with a tendency to form nonlamellar phases, such as phosphatidylethanolamine or cholesterol, stimulates the enzyme even under conditions at which purely lamellar phases exist. Conversely sphingomyelin, a well-known stabilizer of the lamellar phase, inhibits the enzyme. Thus phospholipase C appears to be regulated by the overall geometry and composition of the bilayer.

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Effects of diacylglycerols on the structure of phosphatidylcholine bilayers: a deuterium and phosphorus-31 NMR study

Cited by 80 publications

References 51 publications

Effects of Temperature and Glycerides on the Enhancement of Agkistrodon piscivorus piscivorus Phospholipase A2 Activity by Lysolecithin and Palmitic Acid

Effects of Temperature and Glycerides on the Enhancement of Agkistrodon piscivorus piscivorus Phospholipase A2 Activity by Lysolecithin and Palmitic Acid

Lipid uptake by insect oocytes

Phospholipase C Hydrolysis of Phospholipids in Bilayers of Mixed Lipid Compositions

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